Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship

Marine by-products contain valuable nutrients and there is an increasing interest in production of value-added products for human consumption. Cod (Gadus morhua) head hydrolysates produced by SINTEF Ocean in the pilot project HEADS UP were the base for analyses in this thesis. The hydrolysates were...

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Main Author: Ohnstad, Margrethe Fossheim
Other Authors: Rustad, Turid
Format: Master Thesis
Language:English
Published: NTNU 2018
Subjects:
Online Access:http://hdl.handle.net/11250/2507032
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spelling ftntnutrondheimi:oai:ntnuopen.ntnu.no:11250/2507032 2023-05-15T16:19:08+02:00 Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship Ohnstad, Margrethe Fossheim Rustad, Turid 2018 http://hdl.handle.net/11250/2507032 eng eng NTNU ntnudaim:16319 http://hdl.handle.net/11250/2507032 Bioteknologi (5 årig) Biokjemi og biopolymerkjemi Master thesis 2018 ftntnutrondheimi 2019-09-17T06:54:03Z Marine by-products contain valuable nutrients and there is an increasing interest in production of value-added products for human consumption. Cod (Gadus morhua) head hydrolysates produced by SINTEF Ocean in the pilot project HEADS UP were the base for analyses in this thesis. The hydrolysates were produced from cod harvested in Tufjord in February, March or May of 2017 with varying processing conditions, namely proteolytic enzymes (Bromelain + Papain or Protamex), concentration of enzymes and amount of water. One hydrolysate was produced with stick water, and two of the hydrolysates were added antioxidants. The thesis aimed to measure in vitro ACE inhibitory activity of the hydrolysates, and further investigate structure-activity relationship. All the cod head hydrolysates expressed ACE inhibitory activity in vitro, and IC50 values ranged from 2,60 4,91 mg protein/mL. The antihypertensive effect exerted by one of the hydrolysates was misleading and was therefore not included in this range. Compared to the antihypertensive drug Captopril (IC50 = 0,097 mg/mL), the ACE inhibitory activities of the hydrolysates were found to be relatively low. Four of the hydrolysates were fractionated by ultrafiltration. The fractions enriched in small peptides were found to exert less potent ACE inhibitory activity than the unfractionated hydrolysates. It is therefore suggested that fractionation is unnecessary to increase antihypertensive effects of the cod head hydrolysates. The hydrolysates were composed of amino acids that have been found to contribute to inhibition of ACE, including leucine, isoleucine, valine, phenylalanine and methionine, in addition to a balanced distribution and high content of essential amino acids (average content 38,8  11 %). The hydrolysates contained peptides with broad molecular weight distribution and contained low amounts of free amino acids. No correlation was found between degree of hydrolysis and IC50. No correlations were found between season of harvest and chemical composition of the cod head hydrolysates. Additionally, no correlations were found between processing parameters and ACE inhibitory activity and molecular properties of the hydrolysates. The use of stick water in the production of one hydrolysate did affect the sensory aspects, but not molecular properties. Cod head hydrolysates were found to be a promising potential food ingredient with antihypertensive effects, high solubility, no bitter taste and good nutritional value due to low amounts of free amino acids and high amounts of essential amino acids. Master Thesis Gadus morhua NTNU Open Archive (Norwegian University of Science and Technology) Tufjord ENVELOPE(23.909,23.909,71.005,71.005)
institution Open Polar
collection NTNU Open Archive (Norwegian University of Science and Technology)
op_collection_id ftntnutrondheimi
language English
topic Bioteknologi (5 årig)
Biokjemi og biopolymerkjemi
spellingShingle Bioteknologi (5 årig)
Biokjemi og biopolymerkjemi
Ohnstad, Margrethe Fossheim
Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship
topic_facet Bioteknologi (5 årig)
Biokjemi og biopolymerkjemi
description Marine by-products contain valuable nutrients and there is an increasing interest in production of value-added products for human consumption. Cod (Gadus morhua) head hydrolysates produced by SINTEF Ocean in the pilot project HEADS UP were the base for analyses in this thesis. The hydrolysates were produced from cod harvested in Tufjord in February, March or May of 2017 with varying processing conditions, namely proteolytic enzymes (Bromelain + Papain or Protamex), concentration of enzymes and amount of water. One hydrolysate was produced with stick water, and two of the hydrolysates were added antioxidants. The thesis aimed to measure in vitro ACE inhibitory activity of the hydrolysates, and further investigate structure-activity relationship. All the cod head hydrolysates expressed ACE inhibitory activity in vitro, and IC50 values ranged from 2,60 4,91 mg protein/mL. The antihypertensive effect exerted by one of the hydrolysates was misleading and was therefore not included in this range. Compared to the antihypertensive drug Captopril (IC50 = 0,097 mg/mL), the ACE inhibitory activities of the hydrolysates were found to be relatively low. Four of the hydrolysates were fractionated by ultrafiltration. The fractions enriched in small peptides were found to exert less potent ACE inhibitory activity than the unfractionated hydrolysates. It is therefore suggested that fractionation is unnecessary to increase antihypertensive effects of the cod head hydrolysates. The hydrolysates were composed of amino acids that have been found to contribute to inhibition of ACE, including leucine, isoleucine, valine, phenylalanine and methionine, in addition to a balanced distribution and high content of essential amino acids (average content 38,8  11 %). The hydrolysates contained peptides with broad molecular weight distribution and contained low amounts of free amino acids. No correlation was found between degree of hydrolysis and IC50. No correlations were found between season of harvest and chemical composition of the cod head hydrolysates. Additionally, no correlations were found between processing parameters and ACE inhibitory activity and molecular properties of the hydrolysates. The use of stick water in the production of one hydrolysate did affect the sensory aspects, but not molecular properties. Cod head hydrolysates were found to be a promising potential food ingredient with antihypertensive effects, high solubility, no bitter taste and good nutritional value due to low amounts of free amino acids and high amounts of essential amino acids.
author2 Rustad, Turid
format Master Thesis
author Ohnstad, Margrethe Fossheim
author_facet Ohnstad, Margrethe Fossheim
author_sort Ohnstad, Margrethe Fossheim
title Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship
title_short Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship
title_full Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship
title_fullStr Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship
title_full_unstemmed Marine Cod (Gadus morhua) Head Hydrolysates - in vitro ACE inhibitory activity and investigation of structure-activity relationship
title_sort marine cod (gadus morhua) head hydrolysates - in vitro ace inhibitory activity and investigation of structure-activity relationship
publisher NTNU
publishDate 2018
url http://hdl.handle.net/11250/2507032
long_lat ENVELOPE(23.909,23.909,71.005,71.005)
geographic Tufjord
geographic_facet Tufjord
genre Gadus morhua
genre_facet Gadus morhua
op_relation ntnudaim:16319
http://hdl.handle.net/11250/2507032
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